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Volumn 86, Issue 3, 2013, Pages 367-383

High-resolution optical tweezers for single- molecule manipulation

Author keywords

DNA translocation; Molecular motors; Optical tweezers; Protein folding; Single molecule manipulation; SNARE proteins

Indexed keywords

MOLECULAR MOTOR; PIL PROTEIN; PROTEIN VARIANT; SNARE PROTEIN; UNCLASSIFIED DRUG;

EID: 84884489509     PISSN: 00440086     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (46)

References (129)
  • 2
    • 4243504131 scopus 로고
    • Acceleration and trapping of particles by radiation pressure
    • Ashkin A. Acceleration and trapping of particles by radiation pressure. Phys Rev Lett. 1970;24(4):156-9.
    • (1970) Phys Rev Lett. , vol.24 , Issue.4 , pp. 156-159
    • Ashkin, A.1
  • 3
    • 0022655537 scopus 로고
    • Observation of a single-beam gradient force optical trap for dielectric particles
    • Ashkin A, Dziedzic JM, Bjorkholm JE, Chu S. Observation of a single-beam gradient force optical trap for dielectric particles. Opt Lett. 1986;11(5):288.
    • (1986) Opt Lett. , vol.11 , Issue.5 , pp. 288
    • Ashkin, A.1    Dziedzic, J.M.2    Bjorkholm, J.E.3    Chu, S.4
  • 5
    • 79957848754 scopus 로고    scopus 로고
    • Optical tweezers study life under tension
    • Fazal FM, Block SM. Optical tweezers study life under tension. Nat Photonics. 2011;5(6):318-21.
    • (2011) Nat Photonics. , vol.5 , Issue.6 , pp. 318-321
    • Fazal, F.M.1    Block, S.M.2
  • 7
    • 30144436268 scopus 로고    scopus 로고
    • RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP
    • Dumont S, Cheng W, Serebrov V, Beran RK, Tinoco I, Pyle AM, et al. RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP. Nature. 2006;439(7072):105-8.
    • (2006) Nature. , vol.439 , Issue.7072 , pp. 105-108
    • Dumont, S.1    Cheng, W.2    Serebrov, V.3    Beran, R.K.4    Tinoco, I.5    Pyle, A.M.6
  • 8
    • 33947638345 scopus 로고    scopus 로고
    • DNA translocation and loop formation mechanism of chromatin remodeling by SWI/SNF and RSC
    • Zhang YL, Smith CL, Saha A, Grill SW, Mihardja S, Smith SB, et al. DNA translocation and loop formation mechanism of chromatin remodeling by SWI/SNF and RSC. Mol Cell. 2006;24(4):559-68.
    • (2006) Mol Cell. , vol.24 , Issue.4 , pp. 559-568
    • Zhang, Y.L.1    Smith, C.L.2    Saha, A.3    Grill, S.W.4    Mihardja, S.5    Smith, S.B.6
  • 9
    • 79955534260 scopus 로고    scopus 로고
    • ClpX(P) generates mechanical force to unfold and translocate its protein substrates
    • Maillard RA, Chistol G, Sen M, Righini M, Tan J, Kaiser CM, et al. ClpX(P) generates mechanical force to unfold and translocate its protein substrates. Cell. 2011;145(3):459-69.
    • (2011) Cell. , vol.145 , Issue.3 , pp. 459-469
    • Maillard, R.A.1    Chistol, G.2    Sen, M.3    Righini, M.4    Tan, J.5    Kaiser, C.M.6
  • 10
    • 79953888421 scopus 로고    scopus 로고
    • Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine
    • Aubin-Tam ME, Olivares AO, Sauer RT, Baker TA, Lang MJ. Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine. Cell. 2011;145(2):257-67.
    • (2011) Cell. , vol.145 , Issue.2 , pp. 257-267
    • Aubin-Tam, M.E.1    Olivares, A.O.2    Sauer, R.T.3    Baker, T.A.4    Lang, M.J.5
  • 11
    • 84869009900 scopus 로고    scopus 로고
    • Nucleosomal elements that control the topography of the barrier to transcription
    • Bintu L, Ishibashi T, Dangkulwanich M, Wu YY, Lubkowska L, Kashlev M, et al. Nucleosomal elements that control the topography of the barrier to transcription. Cell. 2012;151(4):738-49.
    • (2012) Cell. , vol.151 , Issue.4 , pp. 738-749
    • Bintu, L.1    Ishibashi, T.2    Dangkulwanich, M.3    Wu, Y.Y.4    Lubkowska, L.5    Kashlev, M.6
  • 12
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studied with optical tweezers
    • Block SM, Goldstein LSB, Schnapp BJ. Bead movement by single kinesin molecules studied with optical tweezers. Nature. 1990;348(6299):348-52.
    • (1990) Nature. , vol.348 , Issue.6299 , pp. 348-352
    • Block, S.M.1    Goldstein, L.S.B.2    Schnapp, B.J.3
  • 13
    • 0033536183 scopus 로고    scopus 로고
    • Single kinesin molecules studied with a molecular force clamp
    • Visscher K, Schnitzer MJ, Block SM. Single kinesin molecules studied with a molecular force clamp. Nature. 1999;400(6740):184-9.
    • (1999) Nature. , vol.400 , Issue.6740 , pp. 184-189
    • Visscher, K.1    Schnitzer, M.J.2    Block, S.M.3
  • 14
    • 0347623370 scopus 로고    scopus 로고
    • Kinesin moves by an asymmetric hand-over-hand mechanism
    • Asbury CL, Fehr AN, Block SM. Kinesin moves by an asymmetric hand-over-hand mechanism. Science. 2003;302(5653):2130-4.
    • (2003) Science. , vol.302 , Issue.5653 , pp. 2130-2134
    • Asbury, C.L.1    Fehr, A.N.2    Block, S.M.3
  • 15
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics-piconewton forces and nanometer steps
    • Finer JT, Simmons RM, Spudich JA. Single myosin molecule mechanics-piconewton forces and nanometer steps. Nature. 1994;368(6467):113-9.
    • (1994) Nature. , vol.368 , Issue.6467 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 16
  • 17
    • 34147206187 scopus 로고    scopus 로고
    • Backtracking determines the force sensitivity of RNAP II in a factor-dependent manner
    • Galburt EA, Grill SW, Wiedmann A, Lubkowska L, Choy J, Nogales E, et al. Backtracking determines the force sensitivity of RNAP II in a factor-dependent manner. Nature. 2007;446(7137):820-3.
    • (2007) Nature. , vol.446 , Issue.7137 , pp. 820-823
    • Galburt, E.A.1    Grill, S.W.2    Wiedmann, A.3    Lubkowska, L.4    Choy, J.5    Nogales, E.6
  • 18
    • 0034594940 scopus 로고    scopus 로고
    • Single-molecule studies of the effect of template tension on T7 DNA polymerase activity
    • Wuite GJ, Smith SB, Young M, Keller D, Bustamante C. Single-molecule studies of the effect of template tension on T7 DNA polymerase activity. Nature. 2000;404(6773):103-6.
    • (2000) Nature. , vol.404 , Issue.6773 , pp. 103-106
    • Wuite, G.J.1    Smith, S.B.2    Young, M.3    Keller, D.4    Bustamante, C.5
  • 19
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage phi 29 portal motor can package DNA against a large internal force
    • Smith DE, Tans SJ, Smith SB, Grimes S, Anderson DL, Bustamante C. The bacteriophage phi 29 portal motor can package DNA against a large internal force. Nature. 2001;413(6857):748-52.
    • (2001) Nature. , vol.413 , Issue.6857 , pp. 748-752
    • Smith, D.E.1    Tans, S.J.2    Smith, S.B.3    Grimes, S.4    Anderson, D.L.5    Bustamante, C.6
  • 20
    • 33745498749 scopus 로고    scopus 로고
    • Visualization of Rad54, a chromatin remodeling protein, translocating on single DNA molecules
    • Amitani I, Baskin RJ, Kowalczykowski SC. Visualization of Rad54, a chromatin remodeling protein, translocating on single DNA molecules. Mol Cell. 2006;23:143-8.
    • (2006) Mol Cell. , vol.23 , pp. 143-148
    • Amitani, I.1    Baskin, R.J.2    Kowalczykowski, S.C.3
  • 21
    • 79958858041 scopus 로고    scopus 로고
    • The RSC chromatin remodeling ATPase translocates DNA with high force and small step size
    • Sirinakis G, Clapier CR, Gao Y, Viswanathanc R, Cairns BR, Zhang YL. The RSC chromatin remodeling ATPase translocates DNA with high force and small step size. EMBO J. 2011;30:2364-72.
    • (2011) EMBO J. , vol.30 , pp. 2364-2372
    • Sirinakis, G.1    Clapier, C.R.2    Gao, Y.3    Viswanathanc, R.4    Cairns, B.R.5    Zhang, Y.L.6
  • 23
    • 0035905687 scopus 로고    scopus 로고
    • Processive translocation and DNA unwinding by individual RecBCD enzyme molecules
    • Bianco PR, Brewer LR, Corzett M, Balhorn R, Yeh Y, Kowalczykowski SC, et al. Processive translocation and DNA unwinding by individual RecBCD enzyme molecules. Nature. 2001;409(6818):374-8.
    • (2001) Nature. , vol.409 , Issue.6818 , pp. 374-378
    • Bianco, P.R.1    Brewer, L.R.2    Corzett, M.3    Balhorn, R.4    Yeh, Y.5    Kowalczykowski, S.C.6
  • 26
    • 34250766751 scopus 로고    scopus 로고
    • Single-molecule studies reveal dynamics of DNA unwinding by the ringshaped T7 helicase
    • Johnson DS, Bai L, Smith BY, Patel SS, Wang MD. Single-molecule studies reveal dynamics of DNA unwinding by the ringshaped T7 helicase. Cell. 2007;129(7):1299-309.
    • (2007) Cell. , vol.129 , Issue.7 , pp. 1299-1309
    • Johnson, D.S.1    Bai, L.2    Smith, B.Y.3    Patel, S.S.4    Wang, M.D.5
  • 27
    • 33744981369 scopus 로고    scopus 로고
    • Sequence-resolved detecton of pausing by single RNA polymerase molecules
    • Herbert KM, La Porta A, Wong BJ, Mooney RA, Neuman KC, Landick R, et al. Sequence-resolved detecton of pausing by single RNA polymerase molecules. Cell. 2006;125(6):1083-94.
    • (2006) Cell. , vol.125 , Issue.6 , pp. 1083-1094
    • Herbert, K.M.1    la Porta, A.2    Wong, B.J.3    Mooney, R.A.4    Neuman, K.C.5    Landick, R.6
  • 28
    • 0035957720 scopus 로고    scopus 로고
    • Reversible unfolding of single RNA molecules by mechanical force
    • Liphardt J, Onoa B, Smith SB, Tinoco I, Bustamante C. Reversible unfolding of single RNA molecules by mechanical force. Science. 2001;292(5517):733-7.
    • (2001) Science. , vol.292 , Issue.5517 , pp. 733-737
    • Liphardt, J.1    Onoa, B.2    Smith, S.B.3    Tinoco, I.4    Bustamante, C.5
  • 30
    • 35348897239 scopus 로고    scopus 로고
    • Fluorescence-force spectroscopy maps two-dimensional reaction landscape of the Holliday junction
    • Hohng S, Zhou RB, Nahas MK, Yu J, Schulten K, Lilley DMJ, et al. Fluorescence-force spectroscopy maps two-dimensional reaction landscape of the Holliday junction. Science. 2007;318(5848):279-83.
    • (2007) Science. , vol.318 , Issue.5848 , pp. 279-283
    • Hohng, S.1    Zhou, R.B.2    Nahas, M.K.3    Yu, J.4    Schulten, K.5    Lilley, D.M.J.6
  • 31
    • 0242417558 scopus 로고    scopus 로고
    • Identifying kinetic barriers to mechanical unfolding of the T-thermophila ribozyme
    • Onoa B, Dumont S, Liphardt J, Smith SB, Tinoco I, Bustamante C. Identifying kinetic barriers to mechanical unfolding of the T-thermophila ribozyme. Science. 2003;299(5614):1892-5.
    • (2003) Science. , vol.299 , Issue.5614 , pp. 1892-1895
    • Onoa, B.1    Dumont, S.2    Liphardt, J.3    Smith, S.B.4    Tinoco, I.5    Bustamante, C.6
  • 32
    • 38849204944 scopus 로고    scopus 로고
    • Direct observation of hierarchical folding in single riboswitch aptamers
    • Greenleaf WJ, Frieda KL, Foster DAN, Woodside MT, Block SM. Direct observation of hierarchical folding in single riboswitch aptamers. Science. 2008;319(5863):630-3.
    • (2008) Science. , vol.319 , Issue.5863 , pp. 630-633
    • Greenleaf, W.J.1    Frieda, K.L.2    Foster, D.A.N.3    Woodside, M.T.4    Block, S.M.5
  • 33
  • 34
    • 25444512161 scopus 로고    scopus 로고
    • Direct observation of the three-state folding of a single protein molecule
    • Cecconi C, Shank EA, Bustamante C, Marqusee S. Direct observation of the three-state folding of a single protein molecule. Science. 2005;309(5743):2057-60.
    • (2005) Science. , vol.309 , Issue.5743 , pp. 2057-2060
    • Cecconi, C.1    Shank, E.A.2    Bustamante, C.3    Marqusee, S.4
  • 35
    • 77953231020 scopus 로고    scopus 로고
    • The folding cooperativity of a protein is controlled by its chain topology
    • Shank EA, Cecconi C, Dill JW, Marqusee S, Bustamante C. The folding cooperativity of a protein is controlled by its chain topology. Nature. 2010;465(7298):637-40.
    • (2010) Nature. , vol.465 , Issue.7298 , pp. 637-640
    • Shank, E.A.1    Cecconi, C.2    Dill, J.W.3    Marqusee, S.4    Bustamante, C.5
  • 36
    • 76649093956 scopus 로고    scopus 로고
    • Full distance-resolved folding energy landscape of one single protein molecule
    • Gebhardt JCM, Bornschlogla T, Rief M. Full distance-resolved folding energy landscape of one single protein molecule. Proc Natl Acad Sci USA. 2010;107(5):2013-8.
    • (2010) Proc Natl Acad Sci USA. , vol.107 , Issue.5 , pp. 2013-2018
    • Gebhardt, J.C.M.1    Bornschlogla, T.2    Rief, M.3
  • 37
    • 80051580720 scopus 로고    scopus 로고
    • Highly anisotropic stability and folding kinetics of a single coiled coil protein under mechanical tension
    • Gao Y, Sirinakis G, Zhang YL. Highly anisotropic stability and folding kinetics of a single coiled coil protein under mechanical tension. J Am Chem Soc. 2011;133:12749-57.
    • (2011) J Am Chem Soc. , vol.133 , pp. 12749-12757
    • Gao, Y.1    Sirinakis, G.2    Zhang, Y.L.3
  • 38
    • 80055087629 scopus 로고    scopus 로고
    • The complex folding network of single calmodulin molecules
    • Stigler J, Ziegler F, Gieseke A, Gebhardt JCM, Rief M. The complex folding network of single calmodulin molecules. Science. 2011;334(6055):512-6.
    • (2011) Science. , vol.334 , Issue.6055 , pp. 512-516
    • Stigler, J.1    Ziegler, F.2    Gieseke, A.3    Gebhardt, J.C.M.4    Rief, M.5
  • 39
    • 66749099068 scopus 로고    scopus 로고
    • Mechanoenzymatic cleavage of the ultralarge vascular protein von Willebrand factor
    • Zhang XH, Halvorsen K, Zhang CZ, Wong WP, Springer TA. Mechanoenzymatic cleavage of the ultralarge vascular protein von Willebrand factor. Science. 2009;324(5932):1330-4.
    • (2009) Science. , vol.324 , Issue.5932 , pp. 1330-1334
    • Zhang, X.H.1    Halvorsen, K.2    Zhang, C.Z.3    Wong, W.P.4    Springer, T.A.5
  • 40
    • 84870381713 scopus 로고    scopus 로고
    • Dynamic force sensing of filamin revealed in single-molecule experiments
    • Rognoni L, Stigler J, Pelz B, Ylanne J, Rief M. Dynamic force sensing of filamin revealed in single-molecule experiments. Proc Natl Acad Sci USA. 2012;109(48):19679-84.
    • (2012) Proc Natl Acad Sci USA. , vol.109 , Issue.48 , pp. 19679-19684
    • Rognoni, L.1    Stigler, J.2    Pelz, B.3    Ylanne, J.4    Rief, M.5
  • 41
    • 84859465192 scopus 로고    scopus 로고
    • Direct observation of multiple misfolding pathways in a single prion protein molecule
    • Yu H, Liu X, Neupane K, Gupta AN, Brigley AM, Solanki A, et al. Direct observation of multiple misfolding pathways in a single prion protein molecule. Proc Natl Acad Sci USA. 2012;109(14):5283-8.
    • (2012) Proc Natl Acad Sci USA. , vol.109 , Issue.14 , pp. 5283-5288
    • Yu, H.1    Liu, X.2    Neupane, K.3    Gupta, A.N.4    Brigley, A.M.5    Solanki, A.6
  • 42
    • 84867498851 scopus 로고    scopus 로고
    • A highly compliant protein native state with a spontaneous-like mechanical unfolding pathway
    • Heidarsson PO, Valpapuram I, Camilloni C, Imparato A, Tiana G, Poulsen FM, et al. A highly compliant protein native state with a spontaneous-like mechanical unfolding pathway. J Am Chem Soc. 2012;134(41):17068-75.
    • (2012) J Am Chem Soc. , vol.134 , Issue.41 , pp. 17068-17075
    • Heidarsson, P.O.1    Valpapuram, I.2    Camilloni, C.3    Imparato, A.4    Tiana, G.5    Poulsen, F.M.6
  • 43
    • 84866132236 scopus 로고    scopus 로고
    • Single reconstituted neuronal SNARE complexes zipper in three distinct stages
    • Gao Y, Zorman S, Gundersen G, Xi ZQ, Ma L, Sirinakis G, et al. Single reconstituted neuronal SNARE complexes zipper in three distinct stages. Science. 2012;337:1340-3.
    • (2012) Science. , vol.337 , pp. 1340-1343
    • Gao, Y.1    Zorman, S.2    Gundersen, G.3    Xi, Z.Q.4    Ma, L.5    Sirinakis, G.6
  • 45
    • 84859577753 scopus 로고    scopus 로고
    • Direct observation of helix staggering, sliding, and coiled coil misfolding
    • Xi ZQ, Gao Y, Sirinakis G, Guo HL, Zhang YL. Direct observation of helix staggering, sliding, and coiled coil misfolding. Proc Natl Acad Sci USA. 2012;109(15):5711-6.
    • (2012) Proc Natl Acad Sci USA. , vol.109 , Issue.15 , pp. 5711-5716
    • Xi, Z.Q.1    Gao, Y.2    Sirinakis, G.3    Guo, H.L.4    Zhang, Y.L.5
  • 49
    • 0034602688 scopus 로고    scopus 로고
    • Pulling a single chromatin fiber reveals the forces that maintain its higher-order structure
    • Cui Y, Bustamante C. Pulling a single chromatin fiber reveals the forces that maintain its higher-order structure. Proc Natl Acad Sci USA. 2000;97(1):127-32.
    • (2000) Proc Natl Acad Sci USA. , vol.97 , Issue.1 , pp. 127-132
    • Cui, Y.1    Bustamante, C.2
  • 50
    • 0033621088 scopus 로고    scopus 로고
    • Polymerization and mechanical properties of single RecA-DNA filaments
    • Hegner M, Smith SB, Bustamante C. Polymerization and mechanical properties of single RecA-DNA filaments. Proc Natl Acad Sci USA. 1999;96(18):10109-14.
    • (1999) Proc Natl Acad Sci USA. , vol.96 , Issue.18 , pp. 10109-10114
    • Hegner, M.1    Smith, S.B.2    Bustamante, C.3
  • 51
    • 59649116344 scopus 로고    scopus 로고
    • Counting RAD51 proteins disassembling from nucleoprotein filaments under tension
    • van Mameren J, Modesti M, Kanaar R, Wyman C, Peterman EJ, Wuite GJ. Counting RAD51 proteins disassembling from nucleoprotein filaments under tension. Nature. 2009;457(7230):745-8.
    • (2009) Nature. , vol.457 , Issue.7230 , pp. 745-748
    • van Mameren, J.1    Modesti, M.2    Kanaar, R.3    Wyman, C.4    Peterman, E.J.5    Wuite, G.J.6
  • 52
    • 33751098486 scopus 로고    scopus 로고
    • Bacterial chromatin organization by H-NS protein unravelled using dual DNA manipulation
    • Dame RT, Noom MC, Wuite GJL. Bacterial chromatin organization by H-NS protein unravelled using dual DNA manipulation. Nature. 2006;444(7117):387-90.
    • (2006) Nature. , vol.444 , Issue.7117 , pp. 387-390
    • Dame, R.T.1    Noom, M.C.2    Wuite, G.J.L.3
  • 53
    • 79960804204 scopus 로고    scopus 로고
    • SSB functions as a sliding platform that migrates on DNA via reptation
    • Zhou R, Kozlov AG, Roy R, Zhang J, Korolev S, Lohman TM, et al. SSB functions as a sliding platform that migrates on DNA via reptation. Cell. 2011;146(2):222-32.
    • (2011) Cell. , vol.146 , Issue.2 , pp. 222-232
    • Zhou, R.1    Kozlov, A.G.2    Roy, R.3    Zhang, J.4    Korolev, S.5    Lohman, T.M.6
  • 54
    • 33745162550 scopus 로고    scopus 로고
    • Differential detection of dual traps improves the spatial resolution of optical tweezers
    • Moffitt JR, Chemla YR, Izhaky D, Bustamante C. Differential detection of dual traps improves the spatial resolution of optical tweezers. Proc Natl Acad Sci USA. 2006;103(24):9006-11.
    • (2006) Proc Natl Acad Sci USA. , vol.103 , Issue.24 , pp. 9006-9011
    • Moffitt, J.R.1    Chemla, Y.R.2    Izhaky, D.3    Bustamante, C.4
  • 56
    • 52149114343 scopus 로고    scopus 로고
    • High-resolution dual-trap optical tweezers with differential detection
    • In: Selvin PR, Ha T, editors, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Bustamante C, Chemla YR, Moffitt JR. High-resolution dual-trap optical tweezers with differential detection. In: Selvin PR, Ha T, editors. Single-Molecule Techniques: A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press; 2008. p. 297-324.
    • (2008) Single-Molecule Techniques: A Laboratory Manual , pp. 297-324
    • Bustamante, C.1    Chemla, Y.R.2    Moffitt, J.R.3
  • 57
    • 0002374601 scopus 로고    scopus 로고
    • Interference model for back-focal-plane displacement detection in optical tweezers
    • Gittes F, Schmidt CF. Interference model for back-focal-plane displacement detection in optical tweezers. Optics Letters. 1998;23(1):7-9.
    • (1998) Optics Letters. , vol.23 , Issue.1 , pp. 7-9
    • Gittes, F.1    Schmidt, C.F.2
  • 59
    • 79953292607 scopus 로고    scopus 로고
    • Ultrahighresolution optical trap with single-fluorophore sensitivity
    • Comstock MJ, Ha T, Chemla YR. Ultrahighresolution optical trap with single-fluorophore sensitivity. Nat Methods. 2011;8(4):335-40.
    • (2011) Nat Methods. , vol.8 , Issue.4 , pp. 335-340
    • Comstock, M.J.1    Ha, T.2    Chemla, Y.R.3
  • 60
    • 84867012109 scopus 로고    scopus 로고
    • Combined and versatile high-resolution optical tweezers and single-molecule fluorescence microscopy
    • Sirinakis G, Ren YX, Gao Y, Xi ZQ, Zhang YL. Combined and versatile high-resolution optical tweezers and single-molecule fluorescence microscopy. Rev Sci Instrum. 2012;83(9):093708.
    • (2012) Rev Sci Instrum. , vol.83 , Issue.9 , pp. 093708
    • Sirinakis, G.1    Ren, Y.X.2    Gao, Y.3    Xi, Z.Q.4    Zhang, Y.L.5
  • 61
    • 0030024985 scopus 로고    scopus 로고
    • Overstretching B-DNA: The elastic response of individual double-stranded and single-stranded DNA molecules
    • Smith CL, Cui Y, Bustamante C. Overstretching B-DNA: the elastic response of individual double-stranded and single-stranded DNA molecules. Science. 1996;271:795-9.
    • (1996) Science. , vol.271 , pp. 795-799
    • Smith, C.L.1    Cui, Y.2    Bustamante, C.3
  • 62
    • 80053897431 scopus 로고    scopus 로고
    • ATP-induced helicase slippage reveals highly coordinated subunits
    • Sun B, Johnson DS, Patel G, Smith BY, Pandey M, Patel SS, et al. ATP-induced helicase slippage reveals highly coordinated subunits. Nature. 2011;478(7367):132-5.
    • (2011) Nature. , vol.478 , Issue.7367 , pp. 132-135
    • Sun, B.1    Johnson, D.S.2    Patel, G.3    Smith, B.Y.4    Pandey, M.5    Patel, S.S.6
  • 63
    • 84867629183 scopus 로고    scopus 로고
    • Direct observation of cotranscriptional folding in an Adenine riboswitch
    • Frieda KL, Block SM. Direct observation of cotranscriptional folding in an Adenine riboswitch. Science. 2012;338(6105):397-400.
    • (2012) Science. , vol.338 , Issue.6105 , pp. 397-400
    • Frieda, K.L.1    Block, S.M.2
  • 64
    • 0032484096 scopus 로고    scopus 로고
    • Single-molecule enzymatic dynamics
    • Lu HP, Xun LY, Xie XS. Single-molecule enzymatic dynamics. Science. 1998;282(5395):1877-82.
    • (1998) Science. , vol.282 , Issue.5395 , pp. 1877-1882
    • Lu, H.P.1    Xun, L.Y.2    Xie, X.S.3
  • 65
    • 84865453389 scopus 로고    scopus 로고
    • DNA translocation of ATP-dependent chromatin remodelling factors revealed by high-resolution optical tweezers
    • Zhang YL, Sirinakis G, Gundersen G, Xi ZQ, Gao Y. DNA translocation of ATP-dependent chromatin remodelling factors revealed by high-resolution optical tweezers. Methods Enzymol. 2012;513:3-28.
    • (2012) Methods Enzymol. , vol.513 , pp. 3-28
    • Zhang, Y.L.1    Sirinakis, G.2    Gundersen, G.3    Xi, Z.Q.4    Gao, Y.5
  • 66
    • 44449087047 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy: Optical tweezers, magnetic tweezers and atomic force microscopy
    • Neuman KC, Nagy A. Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy. Nat Methods. 2008;5(6):491-505.
    • (2008) Nat Methods. , vol.5 , Issue.6 , pp. 491-505
    • Neuman, K.C.1    Nagy, A.2
  • 67
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M, Gautel M, Oesterhelt F, Fernandez JM, Gaub HE. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 1997;276(5315):1109-12.
    • (1997) Science. , vol.276 , Issue.5315 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 68
    • 1542513548 scopus 로고    scopus 로고
    • Force-clamp spectroscopy monitors the folding trajectory of a single protein
    • Fernandez JM, Li H. Force-clamp spectroscopy monitors the folding trajectory of a single protein. Science. 2004;303(5664):1674-8.
    • (2004) Science. , vol.303 , Issue.5664 , pp. 1674-1678
    • Fernandez, J.M.1    Li, H.2
  • 70
    • 36849080807 scopus 로고    scopus 로고
    • Direct observation of active protein folding using lock-in force spectroscopy
    • Schlierf M, Berkemeier F, Rief M. Direct observation of active protein folding using lock-in force spectroscopy. Biophys J. 2007;93(11):3989-98.
    • (2007) Biophys J. , vol.93 , Issue.11 , pp. 3989-3998
    • Schlierf, M.1    Berkemeier, F.2    Rief, M.3
  • 71
    • 59149096062 scopus 로고    scopus 로고
    • Ligand-dependent equilibrium fluctuations of single Calmodulin molecules
    • Junker JP, Ziegler F, Rief M. Ligand-dependent equilibrium fluctuations of single Calmodulin molecules. Science. 2009;323(5914):633-7.
    • (2009) Science. , vol.323 , Issue.5914 , pp. 633-637
    • Junker, J.P.1    Ziegler, F.2    Rief, M.3
  • 73
    • 0026495432 scopus 로고
    • Direct mechanical measurements of the elasticity of single DNA-molecules by using magnetic beads
    • Smith SB, Finzi L, Bustamante C. Direct mechanical measurements of the elasticity of single DNA-molecules by using magnetic beads. Science. 1992;258(5085):1122-6.
    • (1992) Science. , vol.258 , Issue.5085 , pp. 1122-1126
    • Smith, S.B.1    Finzi, L.2    Bustamante, C.3
  • 75
    • 78751689408 scopus 로고    scopus 로고
    • Improved high-force magnetic tweezers for stretching and fefolding of proteins and short DNA
    • Chen H, Fu HX, Zhu XY, Cong PW, Nakamura F, Yan J. Improved high-force magnetic tweezers for stretching and fefolding of proteins and short DNA. Biophys J. 2011;100(2):517-23.
    • (2011) Biophys J. , vol.100 , Issue.2 , pp. 517-523
    • Chen, H.1    Fu, H.X.2    Zhu, X.Y.3    Cong, P.W.4    Nakamura, F.5    Yan, J.6
  • 78
    • 70449095193 scopus 로고    scopus 로고
    • Characterization of photoactivated singlet oxygen damage in single-molecule optical trap experiments
    • Landry MP, McCall PM, Qi Z, Chemla YR. Characterization of photoactivated singlet oxygen damage in single-molecule optical trap experiments. Biophys J. 2009;97(8):2128-36.
    • (2009) Biophys J. , vol.97 , Issue.8 , pp. 2128-2136
    • Landry, M.P.1    McCall, P.M.2    Qi, Z.3    Chemla, Y.R.4
  • 79
    • 0015859467 scopus 로고
    • Principles that govern folding of protein chains
    • Anfinsen CB. Principles that govern folding of protein chains. Science. 1973;181(4096):223-30.
    • (1973) Science. , vol.181 , Issue.4096 , pp. 223-230
    • Anfinsen, C.B.1
  • 80
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin-Even an ordinary globular protein can assume a rogue guise if conditions are right
    • Fandrich M, Fletcher MA, Dobson CM. Amyloid fibrils from muscle myoglobin-Even an ordinary globular protein can assume a rogue guise if conditions are right. Nature. 2001;410(6825):165-6.
    • (2001) Nature. , vol.410 , Issue.6825 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 81
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M. Molecular chaperones in protein folding and proteostasis. Nature. 2011;475(7356):324-32.
    • (2011) Nature. , vol.475 , Issue.7356 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 83
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg D, Jucker M. The amyloid state of proteins in human diseases. Cell. 2012;148(6):1188-203.
    • (2012) Cell. , vol.148 , Issue.6 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 85
    • 0031285905 scopus 로고    scopus 로고
    • Kinetic partitioning mechanism as a unifying theme in the folding of biomolecules
    • Thirumalai D, Klimov DK, Woodson SA. Kinetic partitioning mechanism as a unifying theme in the folding of biomolecules. Theor Chem Acc. 1997;96(1):14-22.
    • (1997) Theor Chem Acc. , vol.96 , Issue.1 , pp. 14-22
    • Thirumalai, D.1    Klimov, D.K.2    Woodson, S.A.3
  • 87
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: Grappling with SNARE and SM proteins
    • Sudhof TC, Rothman JE. Membrane fusion: Grappling with SNARE and SM proteins. Science. 2009;323(5913):474-7.
    • (2009) Science. , vol.323 , Issue.5913 , pp. 474-477
    • Sudhof, T.C.1    Rothman, J.E.2
  • 89
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deepetch electron microscopy
    • Hanson PI, Roth R, Morisaki H, Jahn R, Heuser JE. Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deepetch electron microscopy. Cell. 1997;90(3):523-35.
    • (1997) Cell. , vol.90 , Issue.3 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 90
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 angstrom resolution
    • Sutton RB, Fasshauer D, Jahn R, Brunger AT. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 angstrom resolution. Nature. 1998;395(6700):347-53.
    • (1998) Nature. , vol.395 , Issue.6700 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 91
    • 0027453868 scopus 로고
    • Direct observation of kinesin stepping by optical trapping interferometry
    • Svoboda K, Schmidt CF, Schnapp BJ, Block SM. Direct observation of kinesin stepping by optical trapping interferometry. Nature. 1993;365(6448):721-7.
    • (1993) Nature. , vol.365 , Issue.6448 , pp. 721-727
    • Svoboda, K.1    Schmidt, C.F.2    Schnapp, B.J.3    Block, S.M.4
  • 92
    • 35348856329 scopus 로고    scopus 로고
    • NS3 helicase actively separates RNA strands and senses sequence barriers ahead of the opening fork
    • Cheng W, Dumont S, Tinoco I, Bustamante C. NS3 helicase actively separates RNA strands and senses sequence barriers ahead of the opening fork. Proc Natl Acad Sci USA. 2007;104(35):13954-9.
    • (2007) Proc Natl Acad Sci USA. , vol.104 , Issue.35 , pp. 13954-13959
    • Cheng, W.1    Dumont, S.2    Tinoco, I.3    Bustamante, C.4
  • 93
    • 67650725820 scopus 로고    scopus 로고
    • The biology of chromatin remodeling complexes
    • Clapier CR, Cairns BR. The biology of chromatin remodeling complexes. Annu Rev Biochem. 2009;78:273-304.
    • (2009) Annu Rev Biochem. , vol.78 , pp. 273-304
    • Clapier, C.R.1    Cairns, B.R.2
  • 94
    • 0037102562 scopus 로고    scopus 로고
    • Chromatin remodeling by RSC involves ATP-dependent DNA translocation
    • Saha A, Wittmeyer J, Cairns BR. Chromatin remodeling by RSC involves ATP-dependent DNA translocation. Genes Dev. 2002;16(16):2120-34.
    • (2002) Genes Dev. , vol.16 , Issue.16 , pp. 2120-2134
    • Saha, A.1    Wittmeyer, J.2    Cairns, B.R.3
  • 96
    • 33746702015 scopus 로고    scopus 로고
    • Interlaced optical force-fluorescence measurements for single molecule biophysics
    • Brau RR, Tarsa PB, Ferrer JM, Lee P, Lang MJ. Interlaced optical force-fluorescence measurements for single molecule biophysics. Biophys J. 2006;91(3):1069-77.
    • (2006) Biophys J. , vol.91 , Issue.3 , pp. 1069-1077
    • Brau, R.R.1    Tarsa, P.B.2    Ferrer, J.M.3    Lee, P.4    Lang, M.J.5
  • 97
    • 34249076359 scopus 로고    scopus 로고
    • Introducing genetically encoded aldehydes into proteins
    • Carrico IS, Carlson BL, Bertozzi CR. Introducing genetically encoded aldehydes into proteins. Nat Chem Biol. 2007;3(6):321-2.
    • (2007) Nat Chem Biol. , vol.3 , Issue.6 , pp. 321-322
    • Carrico, I.S.1    Carlson, B.L.2    Bertozzi, C.R.3
  • 98
    • 27644508250 scopus 로고    scopus 로고
    • Genetically encoded short peptide tag for versatile protein labeling by Sfp phosphopantetheinyl transferase
    • Yin J, Straight PD, McLoughlin SM, Zhou Z, Lin AJ, Golan DE, et al. Genetically encoded short peptide tag for versatile protein labeling by Sfp phosphopantetheinyl transferase. Proc Natl Acad Sci USA. 2005;102(44):15815-20.
    • (2005) Proc Natl Acad Sci USA. , vol.102 , Issue.44 , pp. 15815-15820
    • Yin, J.1    Straight, P.D.2    McLoughlin, S.M.3    Zhou, Z.4    Lin, A.J.5    Golan, D.E.6
  • 99
    • 84864453805 scopus 로고    scopus 로고
    • Click chemistry assisted single-molecule fingerprinting reveals a 3D biomolecular folding funnel
    • Yu ZB, Koirala D, Cui YX, Easterling LF, Zhao Y, Mao HB. Click chemistry assisted single-molecule fingerprinting reveals a 3D biomolecular folding funnel. J Am Chem Soc. 2012;134(30):12338-41.
    • (2012) J Am Chem Soc. , vol.134 , Issue.30 , pp. 12338-12341
    • Yu, Z.B.1    Koirala, D.2    Cui, Y.X.3    Easterling, L.F.4    Zhao, Y.5    Mao, H.B.6
  • 100
    • 84867081368 scopus 로고    scopus 로고
    • A general approach to break the concentration barrier in single-molecule imaging
    • Loveland AB, Habuchi S, Walter JC, van Oijen AM. A general approach to break the concentration barrier in single-molecule imaging. Nat Methods. 2012;9(10):987-92.
    • (2012) Nat Methods. , vol.9 , Issue.10 , pp. 987-992
    • Loveland, A.B.1    Habuchi, S.2    Walter, J.C.3    van Oijen, A.M.4
  • 101
    • 33847672227 scopus 로고    scopus 로고
    • Nanofabricated quartz cylinders for angular trapping: DNA supercoiling torque detection
    • Deufel C, Forth S, Simmons CR, Dejgosha S, Wang MD. Nanofabricated quartz cylinders for angular trapping: DNA supercoiling torque detection. Nat Methods. 2007;4(3):223-5.
    • (2007) Nat Methods. , vol.4 , Issue.3 , pp. 223-225
    • Deufel, C.1    Forth, S.2    Simmons, C.R.3    Dejgosha, S.4    Wang, M.D.5
  • 103
    • 34248190279 scopus 로고    scopus 로고
    • A beta Oligomers-a decade of discovery
    • Walsh DM, Selkoe DJ. A beta Oligomers-a decade of discovery. J Neurochem. 2007;101(5):1172-84.
    • (2007) J Neurochem. , vol.101 , Issue.5 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 104
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • Shankar GM, Li SM, Mehta TH, Garcia-Munoz A, Shepardson NE, Smith I, et al. Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med. 2008;14(8):837-42.
    • (2008) Nat Med. , vol.14 , Issue.8 , pp. 837-842
    • Shankar, G.M.1    Li, S.M.2    Mehta, T.H.3    Garcia-Munoz, A.4    Shepardson, N.E.5    Smith, I.6
  • 106
    • 84866456583 scopus 로고    scopus 로고
    • Preventing Alzheimer's disease
    • Selkoe DJ. Preventing Alzheimer's disease. Science. 2012;337:1488-91.
    • (2012) Science. , vol.337 , pp. 1488-1491
    • Selkoe, D.J.1
  • 107
    • 84862003761 scopus 로고    scopus 로고
    • Expression in Drosophila of tandem amyloid beta peptides provides insights into links between aggregation and neurotoxicity
    • Speretta E, Jahn TR, Tartaglia GG, Favrin G, Barros TP, Imarisio S, et al. Expression in Drosophila of tandem amyloid beta peptides provides insights into links between aggregation and neurotoxicity. J Biol Chem. 2012;287(24):20748-54.
    • (2012) J Biol Chem. , vol.287 , Issue.24 , pp. 20748-20754
    • Speretta, E.1    Jahn, T.R.2    Tartaglia, G.G.3    Favrin, G.4    Barros, T.P.5    Imarisio, S.6
  • 109
    • 0025249842 scopus 로고
    • Membrane-protein folding and oligomerization: The 2-stage model
    • Popot JL, Engelman DM. Membrane-protein folding and oligomerization: the 2-stage model. Biochemistry. 1990;29(17):4031-7.
    • (1990) Biochemistry. , vol.29 , Issue.17 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 110
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White SH, Wimley WC. Membrane protein folding and stability: Physical principles. Annu Rev Biophys Biomol Struct. 1999;28:319-65.
    • (1999) Annu Rev Biophys Biomol Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 111
    • 37249037182 scopus 로고    scopus 로고
    • Molecular code for transmembrane-helix recognition by the Sec61 translocon
    • Hessa T, Meindl-Beinker NM, Bernsel A, Kim H, Sato Y, Lerch-Bader M, et al. Molecular code for transmembrane-helix recognition by the Sec61 translocon. Nature. 2007;450(7172):1026-30.
    • (2007) Nature. , vol.450 , Issue.7172 , pp. 1026-1030
    • Hessa, T.1    Meindl-Beinker, N.M.2    Bernsel, A.3    Kim, H.4    Sato, Y.5    Lerch-Bader, M.6
  • 112
    • 79959928058 scopus 로고    scopus 로고
    • Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers
    • Moon CP, Fleming KG. Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers. Proc Natl Acad Sci USA. 2011;108(25):10174-7.
    • (2011) Proc Natl Acad Sci USA. , vol.108 , Issue.25 , pp. 10174-10177
    • Moon, C.P.1    Fleming, K.G.2
  • 113
    • 49549088809 scopus 로고    scopus 로고
    • Association energetics of membrane spanning alpha-helices
    • MacKenzie KR, Fleming KG. Association energetics of membrane spanning alpha-helices. Curr Opin Struct Biol. 2008;18(4):412-9.
    • (2008) Curr Opin Struct Biol. , vol.18 , Issue.4 , pp. 412-419
    • McKenzie, K.R.1    Fleming, K.G.2
  • 114
    • 78650553544 scopus 로고    scopus 로고
    • Method to measure strong protein-protein interactions in lipid bilayers using a steric trap
    • Hong H, Blois TM, Cao Z, Bowie JU. Method to measure strong protein-protein interactions in lipid bilayers using a steric trap. Proc Natl Acad Sci USA. 2010;107(46):19802-7.
    • (2010) Proc Natl Acad Sci USA. , vol.107 , Issue.46 , pp. 19802-19807
    • Hong, H.1    Blois, T.M.2    Cao, Z.3    Bowie, J.U.4
  • 115
    • 84857650575 scopus 로고    scopus 로고
    • Thermodynamic stability of bacteriorhodopsin mutants measured relative to the bacterioopsin unfolded state
    • Cao Z, Schlebach JP, Park C, Bowie JU. Thermodynamic stability of bacteriorhodopsin mutants measured relative to the bacterioopsin unfolded state. Bba-Biomembranes. 2012;1818(4):1049-54.
    • (2012) Bba-Biomembranes. , vol.1818 , Issue.4 , pp. 1049-1054
    • Cao, Z.1    Schlebach, J.P.2    Park, C.3    Bowie, J.U.4
  • 116
    • 60549094781 scopus 로고    scopus 로고
    • Detergent binding explains anomalous SDS-PAGE migration of membrane proteins
    • Rath A, Glibowicka M, Nadeau VG, Chen G, Deber CM. Detergent binding explains anomalous SDS-PAGE migration of membrane proteins. Proc Natl Acad Sci USA. 2009;106(6):1760-5.
    • (2009) Proc Natl Acad Sci USA. , vol.106 , Issue.6 , pp. 1760-1765
    • Rath, A.1    Glibowicka, M.2    Nadeau, V.G.3    Chen, G.4    Deber, C.M.5
  • 118
    • 1642382983 scopus 로고    scopus 로고
    • Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size
    • Denisov IG, Grinkova YV, Lazarides AA, Sligar SG. Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size. J Am Chem Soc. 2004;126(11):3477-87.
    • (2004) J Am Chem Soc. , vol.126 , Issue.11 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4
  • 119
    • 77951903021 scopus 로고    scopus 로고
    • Membrane protein assembly into Nanodiscs
    • Bayburt TH, Sligar SG. Membrane protein assembly into Nanodiscs. FEBS Lett. 2010;584(9):1721-7.
    • (2010) FEBS Lett. , vol.584 , Issue.9 , pp. 1721-1727
    • Bayburt, T.H.1    Sligar, S.G.2
  • 120
    • 24644450199 scopus 로고    scopus 로고
    • Verification of the Crooks fluctuation theorem and recovery of RNA folding free energies
    • Collin D, Ritort F, Jarzynski C, Smith SB, Tinoco I, Bustamante C. Verification of the Crooks fluctuation theorem and recovery of RNA folding free energies. Nature. 2005;437(7056):231-4.
    • (2005) Nature. , vol.437 , Issue.7056 , pp. 231-234
    • Collin, D.1    Ritort, F.2    Jarzynski, C.3    Smith, S.B.4    Tinoco, I.5    Bustamante, C.6
  • 121
    • 57349124448 scopus 로고    scopus 로고
    • Theory, analysis, and interpretation of single-molecule force spectroscopy experiments
    • Dudko OK, Hummer G, Szabo A. Theory, analysis, and interpretation of single-molecule force spectroscopy experiments. Proc Natl Acad Sci USA. 2008;105(41):15755-60.
    • (2008) Proc Natl Acad Sci USA. , vol.105 , Issue.41 , pp. 15755-15760
    • Dudko, O.K.1    Hummer, G.2    Szabo, A.3
  • 122
    • 84875249565 scopus 로고    scopus 로고
    • From mechanical folding trajectories to intrinsic energy landscapes of biopolymers
    • Hinczewski M, Gebhardt JCM, Rief M, Thirumalai D. From mechanical folding trajectories to intrinsic energy landscapes of biopolymers. Proc Natl Acad Sci USA. 2013;110(12):4500-5.
    • (2013) Proc Natl Acad Sci USA. , vol.110 , Issue.12 , pp. 4500-4505
    • Hinczewski, M.1    Gebhardt, J.C.M.2    Rief, M.3    Thirumalai, D.4
  • 123
    • 0024610919 scopus 로고
    • A tutorial on hidden Markovmodels and selected applications in speech recognition
    • Rabiner LR. A tutorial on hidden Markovmodels and selected applications in speech recognition. Proc IEEE. 1989;77(2):257-86.
    • (1989) Proc IEEE. , vol.77 , Issue.2 , pp. 257-286
    • Rabiner, L.R.1
  • 124
    • 0033808511 scopus 로고    scopus 로고
    • A direct optimization approach to hidden Markov modeling for single channel kinetics
    • Qin F, Auerbach A, Sachs F. A direct optimization approach to hidden Markov modeling for single channel kinetics. Biophys J. 2000;79(4):1915-27.
    • (2000) Biophys J. , vol.79 , Issue.4 , pp. 1915-1927
    • Qin, F.1    Auerbach, A.2    Sachs, F.3
  • 125
    • 33746747438 scopus 로고    scopus 로고
    • Analysis of singlemolecule FRET trajectories using hidden Markov modeling
    • McKinney SA, Joo C, Ha T. Analysis of singlemolecule FRET trajectories using hidden Markov modeling. Biophys J. 2006;91(5):1941-51.
    • (2006) Biophys J. , vol.91 , Issue.5 , pp. 1941-1951
    • McKinney, S.A.1    Joo, C.2    Ha, T.3
  • 126
    • 78649818686 scopus 로고    scopus 로고
    • Improved hidden Markov models for molecular motors. Part 2: Extensions and application to experimental data
    • Syed S, Mullner FE, Selvin PR, Sigworth FJ. Improved hidden Markov models for molecular motors. Part 2: Extensions and application to experimental data. Biophys J. 2010;2010:3696-703.
    • (2010) Biophys J. , vol.2010 , pp. 3696-3703
    • Syed, S.1    Mullner, F.E.2    Selvin, P.R.3    Sigworth, F.J.4
  • 127
    • 78649813624 scopus 로고    scopus 로고
    • Improved hidden Markov models for molecular motors. Part 1: Basic theory
    • Syed S, Mullner FE, Selvin PR, Sigworth FJ. Improved hidden Markov models for molecular motors. Part 1: Basic theory. Biophys J. 2010;99:3684-95.
    • (2010) Biophys J. , vol.99 , pp. 3684-3695
    • Syed, S.1    Mullner, F.E.2    Selvin, P.R.3    Sigworth, F.J.4
  • 129
    • 84868095059 scopus 로고    scopus 로고
    • Calcium-dependent folding of single calmodulin molecules
    • Stigler J, Rief M. Calcium-dependent folding of single calmodulin molecules. Proc Natl Acad Sci USA. 2012;109(44):17814-9.
    • (2012) Proc Natl Acad Sci USA. , vol.109 , Issue.44 , pp. 17814-17819
    • Stigler, J.1    Rief, M.2


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